1f95
From Proteopedia
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| - | [[Image:1f95.png|left|200px]]  | ||
| - | + | ==SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX==  | |
| - | + | <StructureSection load='1f95' size='340' side='right'caption='[[1f95]]' scene=''>  | |
| - | + | == Structural highlights ==  | |
| - | + | <table><tr><td colspan='2'>[[1f95]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F95 FirstGlance]. <br>  | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>  | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f95 OCA], [https://pdbe.org/1f95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f95 RCSB], [https://www.ebi.ac.uk/pdbsum/1f95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f95 ProSAT]</span></td></tr>  | |
| - | ==  | + | </table>  | 
| - | [[1f95]] is a 4 chain structure with sequence from [  | + | == Function ==  | 
| + | [https://www.uniprot.org/uniprot/DYL1_RAT DYL1_RAT] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.  Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.  Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1 (By similarity).  Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (By similarity).  | ||
| + | == Evolutionary Conservation ==  | ||
| + | [[Image:Consurf_key_small.gif|200px|right]]  | ||
| + | Check<jmol>  | ||
| + |   <jmolCheckbox>  | ||
| + |     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f9/1f95_consurf.spt"</scriptWhenChecked>  | ||
| + |     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>  | ||
| + |     <text>to colour the structure by Evolutionary Conservation</text>  | ||
| + |   </jmolCheckbox>  | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f95 ConSurf].  | ||
| + | <div style="clear:both"></div>  | ||
==See Also==  | ==See Also==  | ||
| - | *[[Dynein|Dynein]]  | + | *[[Dynein 3D structures|Dynein 3D structures]]  | 
| - | + | __TOC__  | |
| - | + | </StructureSection>  | |
| - | + | [[Category: Homo sapiens]]  | |
| + | [[Category: Large Structures]]  | ||
[[Category: Rattus norvegicus]]  | [[Category: Rattus norvegicus]]  | ||
| - | [[Category: Fan  | + | [[Category: Fan J-S]]  | 
| - | [[Category: Li  | + | [[Category: Li M]]  | 
| - | [[Category: Tochio  | + | [[Category: Tochio H]]  | 
| - | [[Category: Zhang  | + | [[Category: Zhang M]]  | 
| - | [[Category: Zhang  | + | [[Category: Zhang Q]]  | 
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Current revision
SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX
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Categories: Homo sapiens | Large Structures | Rattus norvegicus | Fan J-S | Li M | Tochio H | Zhang M | Zhang Q

